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1I8H

SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMAN TAU PHOSPHOTHREONINE PEPTIDE

Functional Information from PROSITE/UniProt
site_idPS01159
Number of Residues27
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. WekrmsrssgrvYYfnhitnaSQWERP
ChainResidueDetails
BTRP6-PRO32

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER38

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
AVAL2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by GSK3-beta and PDPK1 => ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO8

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO12

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
AVAL2
ASER11

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 511
ChainResidueDetails

237423

PDB entries from 2025-06-11

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